6WZ6
Complex of mutant (K173M) of Pseudomonas 7A Glutaminase-Asparaginase with L-Glu at pH 5. Covalent acyl-enzyme intermediate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004067 | molecular_function | asparaginase activity |
| A | 0004359 | molecular_function | glutaminase activity |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006528 | biological_process | asparagine metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0050417 | molecular_function | glutamin-(asparagin-)ase activity |
| B | 0004067 | molecular_function | asparaginase activity |
| B | 0004359 | molecular_function | glutaminase activity |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006528 | biological_process | asparagine metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0050417 | molecular_function | glutamin-(asparagin-)ase activity |
| C | 0004067 | molecular_function | asparaginase activity |
| C | 0004359 | molecular_function | glutaminase activity |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0006528 | biological_process | asparagine metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0050417 | molecular_function | glutamin-(asparagin-)ase activity |
| D | 0004067 | molecular_function | asparaginase activity |
| D | 0004359 | molecular_function | glutaminase activity |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0006528 | biological_process | asparagine metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0050417 | molecular_function | glutamin-(asparagin-)ase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue GLU A 400 |
| Chain | Residue |
| A | GLY19 |
| A | SER125 |
| A | HOH583 |
| A | HOH660 |
| B | SER258 |
| B | GLU294 |
| A | THR20 |
| A | TYR34 |
| A | ALA66 |
| A | SER67 |
| A | GLU68 |
| A | GLY99 |
| A | THR100 |
| A | ASP101 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 401 |
| Chain | Residue |
| A | THR116 |
| A | ASP117 |
| A | LYS118 |
| A | GLY154 |
| A | LYS155 |
| A | GLY156 |
| A | THR208 |
| A | HOH623 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue EDO C 401 |
| Chain | Residue |
| C | THR116 |
| C | ASP117 |
| C | GLY154 |
| C | LYS155 |
| C | GLY156 |
| C | HIS207 |
| C | THR208 |
| C | VAL209 |
| C | HOH517 |
| C | HOH588 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO D 401 |
| Chain | Residue |
| D | ARG206 |
| D | GLU212 |
| D | ARG332 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | binding site for Di-peptide GLU B 400 and THR B 20 |
| Chain | Residue |
| A | SER258 |
| A | GLU294 |
| B | GLY19 |
| B | ILE21 |
| B | ALA22 |
| B | GLY23 |
| B | TYR34 |
| B | ALA66 |
| B | SER67 |
| B | GLU68 |
| B | GLY99 |
| B | THR100 |
| B | ASP101 |
| B | SER125 |
| B | ARG127 |
| B | PRO128 |
| B | HOH612 |
| B | HOH642 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | binding site for Di-peptide GLU C 400 and THR C 20 |
| Chain | Residue |
| C | GLY19 |
| C | ILE21 |
| C | ALA22 |
| C | GLY23 |
| C | TYR34 |
| C | ALA66 |
| C | SER67 |
| C | GLU68 |
| C | GLY99 |
| C | THR100 |
| C | ASP101 |
| C | SER125 |
| C | ARG127 |
| C | PRO128 |
| C | HOH579 |
| C | HOH651 |
| D | SER258 |
| D | GLU294 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | binding site for Di-peptide GLU D 400 and THR D 20 |
| Chain | Residue |
| C | SER258 |
| C | GLU294 |
| D | GLY19 |
| D | ILE21 |
| D | ALA22 |
| D | GLY23 |
| D | TYR34 |
| D | ALA66 |
| D | SER67 |
| D | GLU68 |
| D | GLY99 |
| D | THR100 |
| D | ASP101 |
| D | SER125 |
| D | ARG127 |
| D | PRO128 |
| D | HOH589 |
| D | HOH643 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1308 |
| Details | Domain: {"description":"Asparaginase/glutaminase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01068","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10099","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10100","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
